Templating and confining calcium phosphate mineralization within designed protein assemblies
Bone formation involves the deposition of ordered hydroxyapatite (HAp) on collagen fibrils, but the underlying molecular mechanisms remain largely unresolved, limiting the design of protein-apatite hybrid materials. Here we show that computationally designed de novo proteins can template and confine HAp mineralization. We design C3-symmetric oligomers with inner surfaces chemically complementary to the HAp {010} facet, and assemble these through additional interfaces into D3 oligomers, one-dimensional nanotubes, and two-dimensional arrays. Electron microscopy revealed templated mineralization and confinement at each hierarchical level, with mineral shape guided by the underlying protein architecture. Conversion of an initially formed amorphous phase to HAp is driven by the designed protein-mineral interface. Our results establish a framework for programmable protein-guided mineralization, providing a foundation for next-generation hybrid materials.